ID   IDUA_MOUSE              Reviewed;         634 AA.
AC   P48441; E9QM17;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   04-NOV-2026, entry version 159.
DE   RecName: Full=Alpha-L-iduronidase;
DE            EC=3.2.1.76;
DE   Flags: Precursor;
GN   Name=Idua;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX   PubMed=7698753; DOI=10.1006/geno.1994.1621;
RA   Clarke L.A.;
RT   "Murine alpha-L-iduronidase: cDNA isolation and expression.";
RL   Genomics 24:311-316(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Lysosomal hydrolase responsible for the degradation of the
CC       glycosaminoglycans heparan sulfate and dermatan sulfate.
CC       {ECO:0000250|UniProtKB:P35475}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of unsulfated alpha-L-iduronosidic linkages in
CC         dermatan sulfate.; EC=3.2.1.76;
CC         Evidence={ECO:0000269|PubMed:7698753};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P35475}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7698753}.
CC   -!- PTM: N-glycosylation contributes to substrate binding and is required
CC       for full enzymatic activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 39 family. {ECO:0000305}.
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DR   EMBL; L34111; AAC42044.1; -; mRNA.
DR   EMBL; AC161813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A55683; A55683.
DR   AlphaFoldDB; P48441; -.
DR   SMR; P48441; -.
DR   FunCoup; P48441; 100.
DR   STRING; 10090.ENSMUSP00000071577; -.
DR   CAZy; GH39; Glycoside Hydrolase Family 39.
DR   GlyConnect; P48441; 5 N-Linked glycans (2 sites).
DR   GlyCosmos; P48441; 7 sites, 7 glycans.
DR   GlyGen; P48441; 7 sites, 7 N-linked glycans (3 sites).
DR   iPTMnet; P48441; -.
DR   PhosphoSitePlus; P48441; -.
DR   PaxDb; 10090-ENSMUSP00000071577; -.
DR   PeptideAtlas; P48441; -.
DR   ProteomicsDB; 267254; -.
DR   AGR; MGI:96418; -.
DR   MGI; MGI:96418; Idua.
DR   eggNOG; ENOG502QRES; Eukaryota.
DR   InParanoid; P48441; -.
DR   OMA; AAMVWNY; -.
DR   Reactome; R-MMU-2024096; HS-GAG degradation.
DR   Reactome; R-MMU-2024101; CS/DS degradation.
DR   PRO; PR:P48441; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P48441; protein.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0043202; C:lysosomal lumen; IMP:MGI.
DR   GO; GO:0005764; C:lysosome; IMP:MGI.
DR   GO; GO:0003940; F:L-iduronidase activity; IDA:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:GO_Central.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0060348; P:bone development; IMP:MGI.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1990079; P:cartilage homeostasis; IMP:MGI.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR   GO; GO:0048878; P:chemical homeostasis; IMP:MGI.
DR   GO; GO:0030209; P:dermatan sulfate proteoglycan catabolic process; IDA:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR   GO; GO:0006027; P:glycosaminoglycan catabolic process; IDA:MGI.
DR   GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; IMP:MGI.
DR   GO; GO:0030211; P:heparin proteoglycan catabolic process; IDA:MGI.
DR   GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0061037; P:negative regulation of cartilage development; IMP:MGI.
DR   GO; GO:0090341; P:negative regulation of secretion of lysosomal enzymes; IDA:MGI.
DR   GO; GO:0045780; P:positive regulation of bone resorption; IMP:MGI.
DR   GO; GO:0120158; P:positive regulation of collagen catabolic process; IMP:MGI.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   FunFam; 2.60.40.10:FF:001526; Alpha-L-iduronidase; 1.
DR   FunFam; 2.60.40.1500:FF:000001; Alpha-L-iduronidase; 1.
DR   FunFam; 3.20.20.80:FF:000059; Alpha-L-iduronidase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1500; Glycosyl hydrolase domain, family 39; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR049165; GH39_as.
DR   InterPro; IPR049167; GH39_C.
DR   InterPro; IPR049166; GH39_cat.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR000514; Glyco_hydro_39.
DR   InterPro; IPR051923; Glycosyl_Hydrolase_39.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR12631; ALPHA-L-IDURONIDASE; 1.
DR   PANTHER; PTHR12631:SF8; ALPHA-L-IDURONIDASE; 1.
DR   Pfam; PF01229; Glyco_hydro_39; 1.
DR   Pfam; PF21200; Glyco_hydro_39_C; 1.
DR   PRINTS; PR00745; GLHYDRLASE39.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS01027; GLYCOSYL_HYDROL_F39; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW   Reference proteome; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..634
FT                   /note="Alpha-L-iduronidase"
FT                   /id="PRO_0000012201"
FT   ACT_SITE        172
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10068"
FT   ACT_SITE        289
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="alpha-D-mannopyranose"
FT                   /ligand_id="ChEBI:CHEBI:28729"
FT                   /evidence="ECO:0000250|UniProtKB:P35475"
FT   BINDING         46
FT                   /ligand="alpha-D-mannopyranose"
FT                   /ligand_id="ChEBI:CHEBI:28729"
FT                   /evidence="ECO:0000250|UniProtKB:P35475"
FT   BINDING         48
FT                   /ligand="alpha-D-mannopyranose"
FT                   /ligand_id="ChEBI:CHEBI:28729"
FT                   /evidence="ECO:0000250|UniProtKB:P35475"
FT   BINDING         81
FT                   /ligand="alpha-L-iduronate"
FT                   /ligand_id="ChEBI:CHEBI:193037"
FT                   /evidence="ECO:0000250|UniProtKB:P35475"
FT   BINDING         171
FT                   /ligand="alpha-L-iduronate"
FT                   /ligand_id="ChEBI:CHEBI:193037"
FT                   /evidence="ECO:0000250|UniProtKB:P35475"
FT   BINDING         172
FT                   /ligand="alpha-L-iduronate"
FT                   /ligand_id="ChEBI:CHEBI:193037"
FT                   /evidence="ECO:0000250|UniProtKB:P35475"
FT   BINDING         254
FT                   /ligand="alpha-L-iduronate"
FT                   /ligand_id="ChEBI:CHEBI:193037"
FT                   /evidence="ECO:0000250|UniProtKB:P35475"
FT   BINDING         289
FT                   /ligand="alpha-L-iduronate"
FT                   /ligand_id="ChEBI:CHEBI:193037"
FT                   /evidence="ECO:0000250|UniProtKB:P35475"
FT   BINDING         295
FT                   /ligand="alpha-L-iduronate"
FT                   /ligand_id="ChEBI:CHEBI:193037"
FT                   /evidence="ECO:0000250|UniProtKB:P35475"
FT   BINDING         296
FT                   /ligand="alpha-D-mannopyranose"
FT                   /ligand_id="ChEBI:CHEBI:28729"
FT                   /evidence="ECO:0000250|UniProtKB:P35475"
FT   BINDING         339
FT                   /ligand="alpha-L-iduronate"
FT                   /ligand_id="ChEBI:CHEBI:193037"
FT                   /evidence="ECO:0000250|UniProtKB:P35475"
FT   BINDING         353
FT                   /ligand="alpha-L-iduronate"
FT                   /ligand_id="ChEBI:CHEBI:193037"
FT                   /evidence="ECO:0000250|UniProtKB:P35475"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        405
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        531..567
FT                   /evidence="ECO:0000250|UniProtKB:P35475"
FT   CONFLICT        359
FT                   /note="F -> S (in Ref. 1; AAC42044)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        423
FT                   /note="A -> G (in Ref. 1; AAC42044)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   634 AA;  71254 MW;  41A8F5B036B360DB CRC64;
     MLTFFAAFLA APLALAESPY LVRVDAARPL RPLLPFWRST GFCPPLPHDQ ADQYDLSWDQ
     QLNLAYIGAV PHSGIEQVRI HWLLDLITAR KSPGQGLMYN FTHLDAFLDL LMENQLLPGF
     ELMGSPSGYF TDFDDKQQVF EWKDLVSLLA RRYIGRYGLT HVSKWNFETW NEPDHHDFDN
     VSMTTQGFLN YYDACSEGLR IASPTLKLGG PGDSFHPLPR SPMCWSLLGH CANGTNFFTG
     EVGVRLDYIS LHKKGAGSSI AILEQEMAVV EQVQQLFPEF KDTPIYNDEA DPLVGWSLPQ
     PWRADVTYAA LVVKVIAQHQ NLLFANSSSS MRYVLLSNDN AFLSYHPYPF SQRTLTARFQ
     VNNTHPPHVQ LLRKPVLTVM GLMALLDGEQ LWAEVSKAGA VLDSNHTVGV LASTHHPEGS
     AAAWSTTVLI YTSDDTHAHP NHSIPVTLRL RGVPPGLDLV YIVLYLDNQL SSPYSAWQHM
     GQPVFPSAEQ FRRMRMVEDP VAEAPRPFPA RGRLTLHRKL PVPSLLLVHV CTRPLKPPGQ
     VSRLRALPLT HGQLILVWSD ERVGSKCLWT YEIQFSQKGE EYAPINRRPS TFNLFVFSPD
     TAVVSGSYRV RALDYWARPG PFSDPVTYLD VPAS
//